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dc.creatorRossé, Carine-
dc.creatorLodillinsky, Catalina-
dc.creatorFuhrmann, Laetitia-
dc.creatorNourieh, Maya-
dc.creatorMonteiro, Pedro-
dc.creatorIrondelle, Marie-
dc.creatorLagoutte, Emilie-
dc.creatorVacher, Sophie-
dc.creatorWaharte, François-
dc.creatorPaul Gilloteaux, Perrine-
dc.creatorRomao, Maryse-
dc.creatorSengmanivong, Lucie-
dc.creatorLinch, Mark-
dc.creatorVan Lint, Johan-
dc.creatorRaposo, Graça-
dc.creatorVincent Salomon, Anne-
dc.creatorBièche, Ivan-
dc.creatorParker, Peter J.-
dc.creatorChavrier, Philippe-
dc.date2017-05-26T18:44:50Z-
dc.date2017-05-26T18:44:50Z-
dc.date2014-05-
dc.date2017-05-19T18:14:56Z-
dc.date.accessioned2019-04-29T15:35:15Z-
dc.date.available2019-04-29T15:35:15Z-
dc.date.issued2017-05-26T18:44:50Z-
dc.date.issued2017-05-26T18:44:50Z-
dc.date.issued2014-05-
dc.date.issued2017-05-19T18:14:56Z-
dc.identifierRossé, Carine; Lodillinsky, Catalina; Fuhrmann, Laetitia; Nourieh, Maya; Monteiro, Pedro; et al.; Control of MT1-MMP transport by atypical PKC during breast-cancer progression; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 111; 18; 5-2014; 1872-1879-
dc.identifier0027-8424-
dc.identifierhttp://hdl.handle.net/11336/16981-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/297240-
dc.descriptionDissemination of carcinoma cells requires the pericellular degradation of the extracellular matrix, which is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP). In this article, we report a co–up-regulation and colocalization of MT1-MMP and atypical protein kinase C iota (aPKCι) in hormone receptor-negative breast tumors in association with a higher risk of metastasis. Silencing of aPKC in invasive breast-tumor cell lines impaired the delivery of MT1-MMP from late endocytic storage compartments to the surface and inhibited matrix degradation and invasion. We provide evidence that aPKCι, in association with MT1-MMP–containing endosomes, phosphorylates cortactin, which is present in F-actin–rich puncta on MT1-MMP–positive endosomes and regulates cortactin association with the membrane scission protein dynamin-2. Thus, cell line-based observations and clinical data reveal the concerted activity of aPKC, cortactin, and dynamin-2, which control the trafficking of MT1-MMP from late endosome to the plasma membrane and play an important role in the invasive potential of breast-cancer cells. membrane traffic actin cytoskeleton multi-vesicular body MMP14-
dc.descriptionFil: Rossé, Carine. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Lodillinsky, Catalina. Institute Curie; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Fuhrmann, Laetitia. Institute Curie; Francia-
dc.descriptionFil: Nourieh, Maya. Institute Curie; Francia-
dc.descriptionFil: Monteiro, Pedro. Institute Curie; Francia. Universite Pierre et Marie Curie; Francia. Universite de Paris Vi; Francia-
dc.descriptionFil: Irondelle, Marie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Lagoutte, Emilie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Vacher, Sophie. Institute Curie; Francia-
dc.descriptionFil: Waharte, François. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Paul Gilloteaux, Perrine. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Romao, Maryse. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Sengmanivong, Lucie. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Linch, Mark. Cancer Research UK London Research Institute; Reino Unido-
dc.descriptionFil: Van Lint, Johan. Katholikie Universiteit Leuven; Bélgica-
dc.descriptionFil: Raposo, Graça. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.descriptionFil: Vincent Salomon, Anne. Institute Curie; Francia. Katholikie Universiteit Leuven; Bélgica-
dc.descriptionFil: Bièche, Ivan. Institute Curie; Francia-
dc.descriptionFil: Parker, Peter J.. Cancer Research UK London Research Institute; Reino Unido. King’s College London; Reino Unido-
dc.descriptionFil: Chavrier, Philippe. Institute Curie; Francia. Centre National de la Recherche Scientifique; Francia-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherNational Academy of Sciences-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.1400749111-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/111/18/E1872.full-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4020077/-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectBreast cancer-
dc.subjectTumor invasion-
dc.subjectMT1-MMP-
dc.subjectAtypical PKC-
dc.subjectMembrane traffic-
dc.subjectActin cytoskeleton-
dc.subjectMulti vesicular body-
dc.subjectMMP14-
dc.subjectPatología-
dc.subjectMedicina Básica-
dc.subjectCIENCIAS MÉDICAS Y DE LA SALUD-
dc.titleControl of MT1-MMP transport by atypical PKC during breast-cancer progression-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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